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Method for making a biofabricated material containing collagen fibrils

a biofabricated material and collagen technology, applied in the field of biofabricated leather materials, can solve the problems of increasing the cost of leather, and requiring enormous amounts of feed, etc., and achieves the effects of uniform texture, uniform elasticity or tensile strength, and convenient uniform uptake of dyes and coatings

Active Publication Date: 2017-08-17
MODERN MEADOW INC
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Benefits of technology

The invention is about a material made from collagen that can be used in various applications like leather. It is produced by a process where collagen molecules are fibrillated, crosslinked, and lubricated. This material has non-anisotropic physical properties, meaning it is uniform and can be measured in different directions. Unlike natural leather, it has a uniform texture that makes it easier to dye and coat. Its aesthetic appearance is consistent and it can be produced with identical properties on both sides. Overall, this material has improved properties compared to natural leather and can be used in various applications.

Problems solved by technology

However, the raising of livestock requires enormous amounts of feed, pastureland, water, and fossil fuels.
It also produces air and waterway pollution, including production of greenhouse gases like methane.
As the costs of raising livestock rise, the cost of leather will rise.
This slaughter under inhumane conditions is objectionable to many socially conscious people.
Consequently, there is a demand from consumers with ethical, moral or religious objections to the use of natural leather products for products humanely produced without the mistreatment or slaughter of animals or produced in ways that minimize the number of animals slaughtered.
The handling and processing of animal skins into leather also poses health risks because the handling animal skins can expose workers to anthrax and other pathogens and allergens such as those in leather dust.
Animal derived products are also susceptible to contamination with viruses and prions (“mad cow disease”).
Control of the final properties of leather is limited by the natural variation in collagen structure between different animal hides.
The final properties of leather can be controlled to some extent through the incorporation of stabilizing and lubricating molecules into the hide or skin during tanning and retanning, however, the selection of these molecules is limited by the need to penetrate the dense structure of the skin or hide.
Particles as large as several microns in diameter have been incorporated into leather for enhanced lubrication; however, application of these particles is limited to hides with the largest pore sizes.
Uniformly distributing the particles throughout the hide presents many challenges.
Different animals may produce different amino acid compositions of the collagen, which may result in different properties and in differences in the resulting leather.
Plant cells do not naturally produce sufficient amounts of post-translational enzymes to efficiently produce stable collagen.
Highberger does not show that these leather sheets are suitable for commercial use.
Tu describes a sheet of good appearance and feel, but does not show that it is suitable for incorporation into a consumer product.
While fibrillation of soluble collagens and collagen-like proteins has been explored to produce collagen hydrogels for biomedical applications, this technology has not been successfully applied to the production of a material having the strength and aesthetic properties of natural leather.
Attempts to create synthetic leather have come up short in reproducing leather's unique set of functional and aesthetic properties.
While many of these materials have found use in footwear, upholstery, and apparel applications, they have fallen short for luxury application, as they cannot match the breathability, performance, hand feel, or aesthetic properties that make leather so unique and beloved.
To date, no alternative commercial leather-like materials have been made from a uniform network of collagen or collagen-like proteins.
Synthetic plastic materials lack the chemical composition and structure of a collagen network that produces an acceptable leather aesthetic.
While fibrillation of soluble collagens and collagen-like proteins has been explored to bind together ground or comminuted leather scraps or for the production of collagen hydrogels for biomedical applications, harnessing this phenomenon to produce a commercially acceptable leather-like material has not been achieved.

Method used

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  • Method for making a biofabricated material containing collagen fibrils
  • Method for making a biofabricated material containing collagen fibrils
  • Method for making a biofabricated material containing collagen fibrils

Examples

Experimental program
Comparison scheme
Effect test

example 1

Controlling the Thickness of Biofabricated Leather

[0245]Hydrogels of extacted bovine type I collagen were formed at different collagen concentrations and volumes to produce dried collagen materials of different thicknesses. Collagen was dissolved in 0.01N HCl at either 5 g / L or 9 g / L, then 1 part 10× PBS was added to 9 parts dissolved collagen to induce collagen fibrillation and gel formation.

[0246]Solutions of either 0.8 L or 1.6 L of the fibrillating collagen were then cast into molds and incubated at 25° C. to allow hydrogel formation. The 0.8 L solution produced a gel of 1.5 cm thickness while the 1. 7 L solution produced a gel of 3.0 cm thickness. These gels were dehydrated and lubricated in acetone, then dried and mechanically staked into a leather like material. The thickness of the final dried material correlated with the total amount of collagen in the starting hydrogel.

[0247]The thickness of biofabricated leather was controlled by varying its total collagen content. Sample...

example 2

Production of Biofabricated Leather from Type I Collagen

[0248]Type I collagen was purchased from Wuxi Biot Bio-technology Company, ltd. (Medical Collagen Sponge). The collagen was isolated from bovine tendon by acid treatment followed by pepsin digestion, and was purified by size exclusion chromatography, frozen and lyophilized.

[0249]The lyophilized protein (4.1 g) was dissolved in 733 ml 0.01 N HCL using an overhead mixer. After the collagen was adequately dissolved, as evidenced by a lack of solid collagen sponge in the solution (at least lhr mixing at 1600 rpm), 82 uL of the tanning agent Relugan GTW was added to the solution followed by 81 mL of a 10× PBS, pH 11.2 to raise the pH of the solution to 7.2.

[0250]The solution was then mixed for 3 min before pouring the solution into a silicon mold. The collagen solution was incubated in the silicon mold for 2 hrs at 25° C. to allow the collagen to fibrillate into a viscoelastic hydrogel.

[0251]Plateau of rheological properties along w...

example 3

Production of Biofabricated Leather from Type III Collagen

[0256]A solution of recombinant collagen type III at 2.5 mg / ml in 0.01 N HCl (FibroGen, Inc.) was fibrillated by adding 1 part of a 200 mM of sodium phosphate solution (22 mL), pH 11.2 to 9 parts of the collagen solution (200 mL) to increase the pH to 7 and stirred 2 hours at room temperature.

[0257]Fibrillation was confirmed by measuring 400nm absorbance of the solution over time.

[0258]After fibrillation, the fibrils were tanned by adding Relugan GTW (2% w / w offer on the collagen) to the fibril suspension and mixing for 30 min.

[0259]The tanned collagen fibrils were then centrifuged at 3,500 RPM for 30 minutes to concentrate the fibrils to a concentration of 10 mg / ml . The 10 mg / ml fibril pellet was further centrifuged using an ultra-centrifuge at 21,000 RPM for 30 minutes yielding a fibril gel with a concentration of ˜40-50 mg / ml .

[0260]The physical properties of the fibril gel were assessed with a rheometer.

[0261]The storage...

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Abstract

Described herein is a method for producing a biofabricated material from collagen or collagen-like proteins. The collagen or collagen-like proteins are isolated from animal sources or produced by recombinant DNA techniques or by chemical synthesis. The collagen or collagen-like proteins are fibrillated, crosslinked, dehydrated and lubricated thus forming the biofabricated material having a substantially uniform network of collagen fibrils.

Description

CROSS REFERENCE TO RELATED APPLICATIONS[0001]This application claims priority to U.S. Provisional Application No. 62 / 295,435 filed Feb. 15, 2016 and which is incorporated by reference in its entirety. This application is related to U.S. patent application Ser. No. 13 / 853,001, titled “ENGINEERED LEATHER AND METHODS OF MANUFACTURE THEREOF” and filed on Mar. 28, 2013; U.S. patent application Ser. No. 14 / 967,173, titled “ENGINEERED LEATHER AND METHODS OF MANUFACTURE THEREOF” and filed on Dec. 11, 2015; and PCT Patent Application No. PCT / US2015 / 058794, titled “REINFORCED ENGINEERED BIOMATERIALS AND METHODS OF MANUFACTURE THEREOF” and filed on Nov. 3, 2015.BACKGROUND OF THE INVENTION[0002]Field of the Invention[0003]This invention relates to biofabricated leather materials composed of unbundled and randomly-oriented trimeric collagen fibrils that exhibit superior strength, non-anisotropic properties, and uniformity by comparison to conventional leather products, but which have the look, f...

Claims

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Application Information

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Patent Type & Authority Applications(United States)
IPC IPC(8): C08J3/24D04H13/00C14C13/00
CPCC08J3/24C08J2389/06D04H13/00C14C13/00C08L89/06C08L2205/16D04H1/43838D04H1/4382C08L1/02C08L89/00C08L97/02C08L5/04D01F4/00D06N2201/06B32B5/26D06M15/15D06M23/16D06N3/00D06N2203/02D06N7/0097B32B5/022B32B5/024B32B5/026B32B7/12B32B9/025B32B15/02B32B15/14B32B23/10B32B27/12B32B29/02B32B1/08B32B3/266B32B2250/02B32B2250/03B32B2250/20B32B2250/40B32B2250/42B32B2255/02B32B2255/26B32B2262/0207B32B2262/0261B32B2262/0269B32B2262/0276B32B2262/0292B32B2262/04B32B2262/062B32B2262/065B32B2262/067B32B2262/08B32B2262/10B32B2262/101B32B2262/103B32B2262/106B32B2262/14B32B2264/105B32B2307/202B32B2307/208B32B2307/308B32B2307/4026B32B2307/422B32B2307/50B32B2307/51B32B2307/54B32B2307/5825B32B2307/708B32B2307/7265B32B2437/00B32B2437/02B32B2437/04B32B2439/46B32B2451/00B32B2457/00B32B2471/00B32B2479/00B32B2519/00B32B2571/00B32B2601/00B32B2605/003B32B2605/08B32B2605/12B32B2605/18C07K14/78D06N3/0018C08H1/06D06N2211/28D06P3/32C14C9/00C14C9/02D01C3/00D04H1/00D06M15/05D06M2101/06
Inventor PURCELL, BRENDAN PATRICKWILLIAMSON, DAVID THOMASMARGA, FRANCOISE SUZANNESCHOFER, SUSAN J.CASSINGHAM, DARRYL MILES
Owner MODERN MEADOW INC
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